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Crystal structure of mouse PRMT6 with C-terminal tev cleavage site

Analyse Crystal structure of mouse PRMT6 with C-terminal tev cleavage site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SQI
Type: protein
Length: 335 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arginine N-methyltransferase 6
EC: 2.1.1.319
UniProt: Q6NZB1
Ligands: CA
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase 6 (EC 2.1.1.319)	protein	335	28% helix, 34% strand	Q6NZB1

Ligands and binding sites

CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.56	0.90	22	empty
2	122	0.54	0.82	17	empty
3	54	0.42	0.82	14	empty

Compared structures

6SQI · Crystal structure of mouse PRMT6 with C-terminal TEV cleavage site · the same entry in another collection · chain A against A, TM-score 1.00
Q6NZB1 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 6 (Q6NZB1) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6NZB1
Elsewhere: RCSB PDB 6SQI · PDBe 6SQI · UniProt Q6NZB1

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